The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands

EMBO Journal

Volumn 21, Issue 15, 2002, Pages 4196-4205

  Verhoeven, Esther E A ^a   Wyman, Claire ^a   Moolenaar, Geri F ^a   Goosen, Nora ^a  

^a LEIDEN UNIVERSITY   (Netherlands)

Author keywords

Damage recognition; Escherichia coli; Nucleotide excision repair; Scanning force microscopy; UvrB

Indexed keywords

DIMER; MONOMER; PROTEIN; PROTEIN SUBUNIT; PROTEIN UVRAB; PROTEIN UVRB; PROTEIN UVRC; UNCLASSIFIED DRUG;

ARTICLE; DNA STRAND; DNA STRAND BREAKAGE; ESCHERICHIA COLI; EXCISION REPAIR; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; SCANNING FORCE MICROSCOPY;

ADENOSINE TRIPHOSPHATASES; DIMERIZATION; DNA DAMAGE; DNA HELICASES; DNA, BACTERIAL; DNA-BINDING PROTEINS; ENDODEOXYRIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MACROMOLECULAR SUBSTANCES; MICROSCOPY, ATOMIC FORCE; MULTIENZYME COMPLEXES; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SUBUNITS; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036682613     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf396     Document Type: Article

References (24)

1. NMR assignments and secondary structure of the UvrC binding domain of UvrB
2. ATP hydrolysis stimulates binding and release of single-stranded DNA from alternating subunits of the dimeric E. coli Rep helicase
3. Involvement of a cryptic ATPase activity of UvrB and its proteolysis product, UvrB* in DNA repair
4. Introduction of a tryptophan reporter group into the ATP binding motif of the Escherichia coli UvrB protein for the study of nucleotide binding and conformational dynamics
5. Oligomerisation of the UvrB nucleotide excision repair protein of Escherichia coli
6. A two-site kinetic mechanism for ATP binding and hydrolysis by E. coli Rep helicase dimer bound to a single-stranded oligodeoxynucleotide
7. Active site of (A)BC excinuclease. I. Evidence for 5′ incision by UvrC through a catalytic site involving Asp399, Asp438, Asp466 and His538 residues
8. Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus
9. The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3'-incision
10. Function of the homologous regions of the Escherichia coli DNA excision repair proteins UvrB and UvrC in stabilization of the UvrBC-DNA complex and in 3′-incision
11. The role of ATP binding and hydrolysis by UvrB during nucleotide excision repair
12. Clue to damage recognition by UvrB: Residues in the β-hairpin structure prevent binding to non-damaged DNA
13. Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair
14. The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex
15. Molecular mechanism of transcription-repair coupling
16. The β-hairpin of UvrB is essential for DNA binding, damage processing and UvrC mediated incisions
17. Crystal structure of Escherichia coli UvrB C-terminal domain and a model for UvrB-UvrC interaction
18. Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair
19. Nucleotide excision repair in Escherichia coli
20. Catalytic sites for 3′ and 5′ incision of Escherichia coli nucleotide excision repair are both located in UvrC
21. Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition
22. Analysis of UvrABC endonuclease reaction intermediates on cisplatin-damaged DNA using mobility shift gel electrophoresis
23. Unusual oligomerisation required for activity of NtrC, a bacterial enhancer-binding protein